Dmitry Kurouski, Ph.D.
Affiliations: | 2012 | Chemistry | State University of New York, Albany, Albany, NY, United States |
Area:
General Chemistry, Analytical Chemistry, BiochemistryGoogle:
"Dmitry Kurouski"Parents
Sign in to add mentor| Igor K. Lednev | grad student | 2012 | SUNY Albany | |
| (Amyloid Fibril Polymorphism: Structure, Supramolecular Chiraliy and Spontaneous Interconversion.) | ||||
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Publications
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| Ali A, Dou T, Holman AP, et al. (2024) The influence of zwitterionic and anionic phospholipids on protein aggregation. Biophysical Chemistry. 306: 107174 |
| Zhaliazka K, Kurouski D. (2023) Nano-infrared analysis of amyloid β fibrils formed in the presence of lipids with unsaturated fatty acids. Nanoscale. 15: 19650-19657 |
| Rodriguez A, Ali A, Holman AP, et al. (2023) Nanoscale Structural Characterization of Transthyretin Aggregates Formed at Different Time Points of Protein Aggregation Using Atomic Force Microscopy-Infrared Spectroscopy. Protein Science : a Publication of the Protein Society. e4838 |
| Ali A, Zhaliazka K, Holman AP, et al. (2023) Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid. Proteins |
| Ali A, Zhaliazka K, Dou T, et al. (2023) Saturation of fatty acids in phosphatidic acid uniquely alters transthyretin stability changing morphology and toxicity of amyloid fibrils. Chemistry and Physics of Lipids. 257: 105350 |
| Kurouski D. (2023) Elucidating the Role of Lipids in the Aggregation of Amyloidogenic Proteins. Accounts of Chemical Research. 56: 2898-2906 |
| Ali A, Zhaliazka K, Dou T, et al. (2023) Secondary structure and toxicity of transthyretin fibrils can be altered by unsaturated fatty acids. International Journal of Biological Macromolecules. 253: 127241 |
| Joshi R, Zhaliazka K, Holman AP, et al. (2023) Elucidation of the Role of Lipids in Late Endosomes on the Aggregation of Insulin. Acs Chemical Neuroscience. 14: 3551-3559 |
| Frese A, Goode C, Zhaliazka K, et al. (2023) Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils. Protein Science : a Publication of the Protein Society. 32: e4717 |
| Matveyenka M, Zhaliazka K, Kurouski D. (2023) Unsaturated fatty acids uniquely alter aggregation rate of α-synuclein and insulin and change the secondary structure and toxicity of amyloid aggregates formed in their presence. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 37: e22972 |